Affinity separation of lectins using porous membranes immobilized with glycopolymer brushes containing mannose or N-acetyl-D-glucosamine

Yutaro Ogata, Hirokazu Seto, Tatsuya Murakami, Yu Hoshino, Yoshiko Miura

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Porous membranes with glycopolymer brushes were prepared as biomaterials for affinity separation. Glycopolymer brushes contained acrylic acid and D-mannose or N-acetyl-D-glucosamine, and were formed on substrates by surface-initiated atom transfer radical polymerization. The presence of glycopolymer brush was confirmed by X-ray photoelectron spectroscopy, contact angle, and ellipsometry measurements. The interaction between lectin and the glycopolymer immobilized on glass slides was confirmed using fluorescent-labeled proteins. Glycopolymer-immobilized surfaces exhibited specific adsorption of the corresponding lectin, compared with bovine serum albumin. Lectins were continuously rejected by the glycopolymer-immobilized membranes. When the protein solution was permeated through the glycopolymer-immobilized membrane, bovine serum albumin was not adsorbed on the membrane surface. In contrast, concanavalin A and wheat germ agglutinin were rejected by membranes incorporating D-mannose or N-acetyl-D-glucosamine, respectively. The amounts of adsorbed concanavalin A and wheat germ agglutinin was increased five-and two-fold that of adsorbed bovine serum albumin, respectively.

Original languageEnglish
Pages (from-to)169-181
Number of pages13
JournalMembranes
Volume3
Issue number3
DOIs
Publication statusPublished - Jul 30 2013

All Science Journal Classification (ASJC) codes

  • Chemical Engineering (miscellaneous)
  • Process Chemistry and Technology
  • Filtration and Separation

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